2W0T

Solution structure of the FCS zinc finger domain of human LMBL2


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 20 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Solution Structure of the Fcs Zinc Finger Domain of the Human Polycomb Group Protein L(3)Mbt-Like 2.

Lechtenberg, B.C.Allen, M.D.Rutherford, T.J.Freund, S.M.Bycroft, M.

(2009) Protein Sci 18: 657

  • DOI: https://doi.org/10.1002/pro.51
  • Primary Citation of Related Structures:  
    2W0T

  • PubMed Abstract: 

    Polycomb group proteins are epigenetic regulators that maintain patterns of gene expression over multiple rounds of cell division. Many of these proteins, including polyhomeotic and the MBT repeat containing proteins SCM and dSfmbt, contain an atypical C2C2 zinc finger with a characteristic phenylalanine-cysteine-serine sequence motif. The reoccurrence of this so-called FCS zinc finger in a variety of polycomb group proteins suggests that it has an important regulatory function. We have determined the solution structure of the FCS zinc finger of the human dSfmbt homologue L(3)mbt-like 2 (L3MBTL2). The structure consists of a beta-hairpin followed by an alpha-helix. The zinc ligands are situated in the beta-hairpin and at the N-terminus of the alpha-helix an arrangement typical of the treble clef class of zinc fingers. The structure is consistent with the proposal that FCS zinc fingers bind to regulatory RNAs.


  • Organizational Affiliation

    MRC Centre for Protein Engineering, Cambridge, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
LETHAL(3)MALIGNANT BRAIN TUMOR-LIKE 2 PROTEIN43Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q969R5 (Homo sapiens)
Explore Q969R5 
Go to UniProtKB:  Q969R5
PHAROS:  Q969R5
GTEx:  ENSG00000100395 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ969R5
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download Ideal Coordinates CCD File 
B [auth A]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 20 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-01-20
    Type: Initial release
  • Version 1.1: 2017-04-19
    Changes: Other
  • Version 1.2: 2024-05-15
    Changes: Data collection, Database references, Derived calculations, Other